Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

Destruxin B (3R,10R,13S,16S,19S)-16- [(2S)-butan-2-yl]...

Synonyms: AC1L2JVA, NSC 236580, BRN 0601704, 2503-26-6

Chen, H.C. et al., Tsunoo, A. et al., Bradfisch, G.A. et al., Muroi, M. et al., Nakagawa, H. et al., et al.

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Disease relevance of NSC 236580

Suppressive effects of destruxin B on hepatitis B virus surface antigen gene expression in human hepatoma cells [1].

High impact information on NSC 236580

Destruxin B (DestB) and E (DestE), cyclodepsipeptides, were found to inhibit pit formation without affecting osteoclast differentiation and survival [2].
Neither RB, RC, nor DB affected the resting membrane potential or the apparent input resistance of papillary muscles [3].
Acidification of intracellular organelles is also blocked by destruxin B at comparable concentrations when assessed by accumulation of acridine orange [4].
This novel feature of destruxin B should make it a useful probe in the analysis of V-ATPase function in cell physiology [4].
Northern blot analysis indicates that the suppression of HBsAg gene expression by destruxin B is mainly at the mRNA level [1].

Biological context of NSC 236580

Destruxin B not only suppresses the endogenously expressed HBsAg in the Hep3B cells but also suppresses the HBsAg produced either from the stable transfected HBV DNA in another human hepatoma HuH-7 cell line which carry no endogenous HBV genome [1].
We examined the antiviral activity of destruxin B and found that it suppresses the expression of the hepatitis B viral surface antigen (HBsAg) gene in human hepatoma Hep3B cells which carry an integrated viral gene in its chromosome [1].
Crystal and molecular structure of Destruxin B [5].

Anatomical context of NSC 236580

Destruxin A, destruxin B (DB), roseotoxin B (RB), and roseocardin (RC), a novel CDP, each caused a concentration-dependent increase in the contraction force of the right atrium and the papillary and trabecular muscles of the right ventricle at 0.6 to 600 microM [3].
In this study, we have investigated the sensitivity of destruxin B to the voltage-dependent calcium channel antagonists; omega-conotoxin GVIA, nifedipine, diltiazem and methoxyverapamil on skeletal muscle from the lepidopteran insect pest, tobacco budworm (Heliothis virescens) [6].

References

Suppressive effects of destruxin B on hepatitis B virus surface antigen gene expression in human hepatoma cells. Chen, H.C., Chou, C.K., Sun, C.M., Yeh, S.F. Antiviral Res. (1997) [Pubmed]
Destruxins, cyclodepsipeptides, block the formation of actin rings and prominent clear zones and ruffled borders in osteoclasts. Nakagawa, H., Takami, M., Udagawa, N., Sawae, Y., Suda, K., Sasaki, T., Takahashi, N., Wachi, M., Nagai, K., Woo, J.T. Bone (2003) [Pubmed]
Non-cyclic AMP-dependent, positive inotropic cyclodepsipeptides with negative chronotropy. Tsunoo, A., Kamijo, M. J. Pharmacol. Exp. Ther. (1999) [Pubmed]
Destruxin B, a specific and readily reversible inhibitor of vacuolar-type H(+)-translocating ATPase. Muroi, M., Shiragami, N., Takatsuki, A. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
Crystal and molecular structure of Destruxin B. Steiner, J.R., Barnes, C.L. Int. J. Pept. Protein Res. (1988) [Pubmed]
omega-Conotoxin GVIA and nifedipine inhibit the depolarizing action of the fungal metabolite, destruxin B on muscle from the tobacco budworm (Heliothis virescens). Bradfisch, G.A., Harmer, S.L. Toxicon (1990) [Pubmed]

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